Selected article for: "active form and nucleotide analog"
Author: Wanchao Yin; Chunyou Mao; Xiaodong Luan; Dan-Dan Shen; Qingya Shen; Haixia Su; Xiaoxi Wang; Fulai Zhou; Wenfeng Zhao; Minqi Gao; Shenghai Chang; Yuan-Chao Xie; Guanghui Tian; He-Wei Jiang; Sheng-Ce Tao; Jingshan Shen; Yi Jiang; Hualiang Jiang; Yechun Xu; Shuyang Zhang; Yan Zhang; H. Eric Xu
Title: Structural Basis for the Inhibition of the RNA-Dependent RNA Polymerase from SARS-CoV-2 by Remdesivir
  • Document date: 2020_4_9
    • ID: 7v7pzclb_9
    Snippet: At the 3' end of the primer strand is Remdesivir monophosphate (RMP) ( Figure 3C and 4D), which is covalently incorporated into the primer strand at the +1 position ( Figure 4E ). Additional nucleotides at +2 and +3 positions from the template strand from interactions with residues from the back from the index finger subdomain ( Figure 4B ). Despite the presence of excess amount of RTP in complex assembly, only a single RMP is assembled into the .....
    Document: At the 3' end of the primer strand is Remdesivir monophosphate (RMP) ( Figure 3C and 4D), which is covalently incorporated into the primer strand at the +1 position ( Figure 4E ). Additional nucleotides at +2 and +3 positions from the template strand from interactions with residues from the back from the index finger subdomain ( Figure 4B ). Despite the presence of excess amount of RTP in complex assembly, only a single RMP is assembled into the primer strand. Thus, Remdesivir, like many nucleotide analog prodrugs, inhibits the viral RdRp activity indirectly through non-obligate RNA chain termination, a mechanism that requires the conversion of the parent drug to the active triphosphate form (27) .

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